nucleotide pyrophosphatase/triticum aestivum

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Mutational analysis of wheat (Triticum aestivum L.) nucleotide pyrophosphatase/phosphodiesterase shows the role of six amino acids in the catalytic mechanism.

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Nucleotide pyrophosphatases/phosphodiesterases (NPPs, PF01663) release nucleoside 5'-monophosphates from a wide range of nucleotide substrates. Only very recently, the first plant members of the NPP family were characterised (Joye et al. J Cereal Sci 51: 326-336, 2010), and little is known about

Histochemical localization of nucleotide pyrophosphatase and cyclic nucleotide phosphodiesterase in seeds and shoots of Triticum.

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The activities of potato nucleotide pyrophosphatase and cyclic nucleotide phosphodiesterase against a common substrate, p-nitrophenyl thymidine 5'-phosphate and its histochemical analogue, AS-BI-naphthyl thymidine 5'-phosphate, were determined with the aid of relatively specific inhibitors, NAD and

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